ArticleThe Plant cell2012
Two interacting proteins are necessary for the editing of the NdhD-1 site in Arabidopsis plastids.
Article in The Plant cell, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 67 papers.
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Who cites it
67 citing papers in PubMed, 143 citations in OpenAlex.
- Losing genes, gaining edits: how relaxed selection and inverted repeat expansion shape RNA editing in Schizaeaceae plastomes.The Plant journal : for cell and molecular biology · 2026Article
- Structures of pentatricopeptide repeat proteins.Acta crystallographica. Section F, Structural biology communications · 2026Review
- Synthetic Pentatricopeptide Repeat Proteins: Building a Toolkit for Precise RNA Control.International journal of molecular sciences · 2025Review
- High Conservation of Translation-Enabling RNA Editing Sites in Hyper-editing Ferns Implies They Are Not Selectively Neutral.Molecular biology and evolution · 2025Article
- Deciphering the role of accessory proteins in Arabidopsis chloroplast editosomes via interaction with a synthetic PPR-PLS factor in E. coli.Nucleic acids research · 2025Article
- Solid-like condensation of MORF8 inhibits RNA editing under heat stress in Arabidopsis.Nature communications · 2025Article
- Pentatricopeptide repeat proteins in plants: Cellular functions, action mechanisms, and potential applications.Plant communications · 2025Review
- A Conserved Lysine in an Ion-Pair with a Catalytic Glutamate Is Critical for U-to-C RNA Editing but Restricts C-to-U RNA Editing.Biochemistry · 2025Article
- The Roles of MicroRNAs in the Regulation of Rice-Pathogen Interactions.Plants (Basel, Switzerland) · 2025Review
- Applications of Synthetic Pentatricopeptide Repeat Proteins.Plant & cell physiology · 2024Review
- Multiple factors interact in editing of PPR-E+-targeted sites in maize mitochondria and plastids.Plant communications · 2024Article
- Conservation of the moss RNA editing factor PPR78 despite the loss of its known cytidine-to-uridine editing sites is explained by a hidden extra target.The Plant cell · 2024Article
- YUCCA2 (YUC2)-Mediated 3-Indoleacetic Acid (IAA) Biosynthesis Regulates Chloroplast RNA Editing by Relieving the Auxin Response Factor 1 (ARF1)-Dependent Inhibition of Editing Factors inInternational journal of molecular sciences · 2023Article
- Beyond a PPR-RNA recognition code: Many aspects matter for the multi-targeting properties of RNA editing factor PPR56.PLoS genetics · 2023Article
- A ribonuclease activity linked to DYW1 in vitro is inhibited by RIP/MORF proteins.Scientific reports · 2023Article
- Structural insight into the activation of an Arabidopsis organellar C-to-U RNA editing enzyme by active site complementation.The Plant cell · 2023Article
- Plant organellar RNA maturation.The Plant cell · 2023Review
- Maize PPR-E proteins mediate RNA C-to-U editing in mitochondria by recruiting the trans deaminase PCW1.The Plant cell · 2023Article
- Emergence of Novel RNA-Editing Sites by Changes in the Binding Affinity of a Conserved PPR Protein.Molecular biology and evolution · 2022Article
- RNA Editing in Chloroplast: Advancements and Opportunities.Current issues in molecular biology · 2022Review
7 more citing papers are in PubMed but not listed here.
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Authors and funding
9 authors at 5 institutions in 3 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
After transcription, mRNA editing in angiosperm chloroplasts and mitochondria results in the conversion of cytidine to uridine by deamination. Analysis of Arabidopsis thaliana mutants affected in RNA editing have shown that many pentatricopeptide repeat proteins (PPRs) are required for specific cytidine deamination events. PPR proteins have been shown to be sequence-specific RNA binding proteins allowing the recognition of the C to be edited. The C-terminal DYW domain present in many editing factors has been proposed to catalyze C deamination, as it shows sequence similarities with cytidine deaminases in other organisms. However, many editing factors, such as the first to be discovered, CHLORORESPIRATORY REDUCTION4 (CRR4), lack this domain, so its importance has been unclear. Using a reverse genetic approach, we identified DYW1, an RNA editing factor acting specifically on the plastid ndhD-1 editing site recognized by CRR4. Unlike other known editing factors, DYW1 contains no identifiable PPR motifs but does contain a clear DYW domain. We were able to show interaction between CRR4 and DYW1 by bimolecular fluorescence complementation and to reconstitute a functional chimeric CRR4-DYW1 protein complementing the crr4 dyw1double mutant. We propose that CRR4 and DYW1 act together to edit the ndhD-1 site.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.